US4769173A - Enzymatic detergent and bleaching composition - Google Patents
Enzymatic detergent and bleaching composition Download PDFInfo
- Publication number
- US4769173A US4769173A US07/128,256 US12825687A US4769173A US 4769173 A US4769173 A US 4769173A US 12825687 A US12825687 A US 12825687A US 4769173 A US4769173 A US 4769173A
- Authority
- US
- United States
- Prior art keywords
- acid
- lipase
- bleaching agent
- sodium
- lipases
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 40
- 239000003599 detergent Substances 0.000 title claims abstract description 18
- 238000004061 bleaching Methods 0.000 title description 18
- 230000002255 enzymatic effect Effects 0.000 title description 3
- 239000004367 Lipase Substances 0.000 claims abstract description 91
- 108090001060 Lipase Proteins 0.000 claims abstract description 90
- 102000004882 Lipase Human genes 0.000 claims abstract description 90
- 235000019421 lipase Nutrition 0.000 claims abstract description 89
- 239000007844 bleaching agent Substances 0.000 claims abstract description 53
- 229960001922 sodium perborate Drugs 0.000 claims abstract description 19
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 claims abstract description 19
- 150000004965 peroxy acids Chemical class 0.000 claims abstract description 12
- KFSLWBXXFJQRDL-UHFFFAOYSA-N Peracetic acid Chemical compound CC(=O)OO KFSLWBXXFJQRDL-UHFFFAOYSA-N 0.000 claims abstract description 10
- 241000223258 Thermomyces lanuginosus Species 0.000 claims abstract description 7
- 230000002538 fungal effect Effects 0.000 claims abstract description 4
- FRPJTGXMTIIFIT-UHFFFAOYSA-N tetraacetylethylenediamine Chemical compound CC(=O)C(N)(C(C)=O)C(N)(C(C)=O)C(C)=O FRPJTGXMTIIFIT-UHFFFAOYSA-N 0.000 claims description 38
- 102000004190 Enzymes Human genes 0.000 claims description 11
- 108090000790 Enzymes Proteins 0.000 claims description 11
- 108091005804 Peptidases Proteins 0.000 claims description 11
- 239000002243 precursor Substances 0.000 claims description 10
- 102000035195 Peptidases Human genes 0.000 claims description 6
- 230000002366 lipolytic effect Effects 0.000 claims description 6
- 239000002253 acid Substances 0.000 claims description 5
- 229910052783 alkali metal Inorganic materials 0.000 claims description 5
- 239000011149 active material Substances 0.000 claims description 4
- JHUXOSATQXGREM-UHFFFAOYSA-N dodecanediperoxoic acid Chemical compound OOC(=O)CCCCCCCCCCC(=O)OO JHUXOSATQXGREM-UHFFFAOYSA-N 0.000 claims description 4
- 150000004967 organic peroxy acids Chemical class 0.000 claims description 3
- 150000003839 salts Chemical class 0.000 claims description 3
- QSKQNALVHFTOQX-UHFFFAOYSA-M sodium nonanoyloxybenzenesulfonate Chemical compound [Na+].CCCCCCCCC(=O)OC1=CC=CC=C1S([O-])(=O)=O QSKQNALVHFTOQX-UHFFFAOYSA-M 0.000 claims description 3
- GLVYLTSKTCWWJR-UHFFFAOYSA-N 2-carbonoperoxoylbenzoic acid Chemical compound OOC(=O)C1=CC=CC=C1C(O)=O GLVYLTSKTCWWJR-UHFFFAOYSA-N 0.000 claims description 2
- YNJSNEKCXVFDKW-UHFFFAOYSA-N 3-(5-amino-1h-indol-3-yl)-2-azaniumylpropanoate Chemical compound C1=C(N)C=C2C(CC(N)C(O)=O)=CNC2=C1 YNJSNEKCXVFDKW-UHFFFAOYSA-N 0.000 claims description 2
- CKSYEJTXXXFCEV-UHFFFAOYSA-N C1(=CC=CC=C1)S(=O)(=O)OOC(C1=CC=CC=C1)=O.[Na] Chemical compound C1(=CC=CC=C1)S(=O)(=O)OOC(C1=CC=CC=C1)=O.[Na] CKSYEJTXXXFCEV-UHFFFAOYSA-N 0.000 claims description 2
- BPPGLUCINRNKQV-UHFFFAOYSA-N [Na].CC(=O)OOS(=O)(=O)C1=CC=CC=C1 Chemical compound [Na].CC(=O)OOS(=O)(=O)C1=CC=CC=C1 BPPGLUCINRNKQV-UHFFFAOYSA-N 0.000 claims description 2
- SXLLDUPXUVRMEE-UHFFFAOYSA-N nonanediperoxoic acid Chemical compound OOC(=O)CCCCCCCC(=O)OO SXLLDUPXUVRMEE-UHFFFAOYSA-N 0.000 claims description 2
- XWPCPDYPKRDGNE-UHFFFAOYSA-N sodium;(2,3,4-trimethylphenyl) hexanoate Chemical compound [Na].CCCCCC(=O)OC1=CC=C(C)C(C)=C1C XWPCPDYPKRDGNE-UHFFFAOYSA-N 0.000 claims description 2
- DCQJDRNKCUQEMA-UHFFFAOYSA-N tetradecanediperoxoic acid Chemical compound OOC(=O)CCCCCCCCCCCCC(=O)OO DCQJDRNKCUQEMA-UHFFFAOYSA-N 0.000 claims description 2
- 150000004966 inorganic peroxy acids Chemical class 0.000 claims 1
- 230000001580 bacterial effect Effects 0.000 abstract description 4
- 230000037029 cross reaction Effects 0.000 abstract description 4
- 230000001900 immune effect Effects 0.000 abstract description 4
- BGRWYDHXPHLNKA-UHFFFAOYSA-N Tetraacetylethylenediamine Chemical compound CC(=O)N(C(C)=O)CCN(C(C)=O)C(C)=O BGRWYDHXPHLNKA-UHFFFAOYSA-N 0.000 abstract 2
- 229940040461 lipase Drugs 0.000 description 56
- 230000000694 effects Effects 0.000 description 17
- LMYSNFBROWBKMB-UHFFFAOYSA-N 4-[2-(dipropylamino)ethyl]benzene-1,2-diol Chemical compound CCCN(CCC)CCC1=CC=C(O)C(O)=C1 LMYSNFBROWBKMB-UHFFFAOYSA-N 0.000 description 12
- 238000012360 testing method Methods 0.000 description 11
- 229940088598 enzyme Drugs 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 239000004365 Protease Substances 0.000 description 8
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 7
- 241000235527 Rhizopus Species 0.000 description 7
- 239000000427 antigen Substances 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 239000004744 fabric Substances 0.000 description 7
- 238000005406 washing Methods 0.000 description 6
- 241000219198 Brassica Species 0.000 description 5
- 235000003351 Brassica cretica Nutrition 0.000 description 5
- 235000003343 Brassica rupestris Nutrition 0.000 description 5
- 108090000371 Esterases Proteins 0.000 description 5
- 241000589516 Pseudomonas Species 0.000 description 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- QKSKPIVNLNLAAV-UHFFFAOYSA-N bis(2-chloroethyl) sulfide Chemical compound ClCCSCCCl QKSKPIVNLNLAAV-UHFFFAOYSA-N 0.000 description 5
- 238000000034 method Methods 0.000 description 5
- 235000010460 mustard Nutrition 0.000 description 5
- -1 peracetic acid Chemical class 0.000 description 5
- 235000015067 sauces Nutrition 0.000 description 5
- 241000894007 species Species 0.000 description 5
- XSVSPKKXQGNHMD-UHFFFAOYSA-N 5-bromo-3-methyl-1,2-thiazole Chemical compound CC=1C=C(Br)SN=1 XSVSPKKXQGNHMD-UHFFFAOYSA-N 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 108010020132 microbial serine proteinases Proteins 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 239000011734 sodium Substances 0.000 description 4
- 235000019832 sodium triphosphate Nutrition 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 239000000975 dye Substances 0.000 description 3
- 239000000839 emulsion Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000001023 inorganic pigment Substances 0.000 description 3
- 235000019626 lipase activity Nutrition 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- HWGNBUXHKFFFIH-UHFFFAOYSA-I pentasodium;[oxido(phosphonatooxy)phosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O HWGNBUXHKFFFIH-UHFFFAOYSA-I 0.000 description 3
- 229910052708 sodium Inorganic materials 0.000 description 3
- 239000002689 soil Substances 0.000 description 3
- 241000588986 Alcaligenes Species 0.000 description 2
- 229920000742 Cotton Polymers 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 241000235395 Mucor Species 0.000 description 2
- 235000019482 Palm oil Nutrition 0.000 description 2
- 241000235403 Rhizomucor miehei Species 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 239000004115 Sodium Silicate Substances 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 150000001340 alkali metals Chemical class 0.000 description 2
- 125000000129 anionic group Chemical group 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000004453 electron probe microanalysis Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 150000004682 monohydrates Chemical class 0.000 description 2
- KJPHTXTWFHVJIG-UHFFFAOYSA-N n-ethyl-2-[(6-methoxypyridin-3-yl)-(2-methylphenyl)sulfonylamino]-n-(pyridin-3-ylmethyl)acetamide Chemical compound C=1C=C(OC)N=CC=1N(S(=O)(=O)C=1C(=CC=CC=1)C)CC(=O)N(CC)CC1=CC=CN=C1 KJPHTXTWFHVJIG-UHFFFAOYSA-N 0.000 description 2
- 239000002540 palm oil Substances 0.000 description 2
- 239000002304 perfume Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 150000003138 primary alcohols Chemical class 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000000344 soap Substances 0.000 description 2
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 2
- 229910052911 sodium silicate Inorganic materials 0.000 description 2
- HFQQZARZPUDIFP-UHFFFAOYSA-M sodium;2-dodecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCC1=CC=CC=C1S([O-])(=O)=O HFQQZARZPUDIFP-UHFFFAOYSA-M 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 239000000375 suspending agent Substances 0.000 description 2
- 239000000271 synthetic detergent Substances 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- JBNHKYQZNSPSOR-UHFFFAOYSA-N 4-(carboxymethylperoxy)-4-oxobutanoic acid Chemical class OC(=O)CCC(=O)OOCC(O)=O JBNHKYQZNSPSOR-UHFFFAOYSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- 244000215068 Acacia senegal Species 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000589513 Burkholderia cepacia Species 0.000 description 1
- 229910021532 Calcite Inorganic materials 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 229920000084 Gum arabic Polymers 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 241000729876 Niveus Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 102000019280 Pancreatic lipases Human genes 0.000 description 1
- 108050006759 Pancreatic lipases Proteins 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 241000364057 Peoria Species 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 229930182556 Polyacetal Natural products 0.000 description 1
- 241000589540 Pseudomonas fluorescens Species 0.000 description 1
- 241000589538 Pseudomonas fragi Species 0.000 description 1
- 241000145542 Pseudomonas marginata Species 0.000 description 1
- 241000204735 Pseudomonas nitroreducens Species 0.000 description 1
- 241000589774 Pseudomonas sp. Species 0.000 description 1
- 235000019484 Rapeseed oil Nutrition 0.000 description 1
- 241000698291 Rugosa Species 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 241000223257 Thermomyces Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 239000004904 UV filter Substances 0.000 description 1
- 239000000205 acacia gum Substances 0.000 description 1
- 235000010489 acacia gum Nutrition 0.000 description 1
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 229910000288 alkali metal carbonate Inorganic materials 0.000 description 1
- 150000008041 alkali metal carbonates Chemical class 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 230000003625 amylolytic effect Effects 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- SRSXLGNVWSONIS-UHFFFAOYSA-M benzenesulfonate Chemical compound [O-]S(=O)(=O)C1=CC=CC=C1 SRSXLGNVWSONIS-UHFFFAOYSA-M 0.000 description 1
- VAIFPCUQBLOXJW-UHFFFAOYSA-N benzenesulfonyl benzenecarboperoxoate Chemical compound C=1C=CC=CC=1C(=O)OOS(=O)(=O)C1=CC=CC=C1 VAIFPCUQBLOXJW-UHFFFAOYSA-N 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 150000007942 carboxylates Chemical class 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 229960001484 edetic acid Drugs 0.000 description 1
- NFDRPXJGHKJRLJ-UHFFFAOYSA-N edtmp Chemical compound OP(O)(=O)CN(CP(O)(O)=O)CCN(CP(O)(O)=O)CP(O)(O)=O NFDRPXJGHKJRLJ-UHFFFAOYSA-N 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 229940116369 pancreatic lipase Drugs 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 239000003208 petroleum Substances 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920006324 polyoxymethylene Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 102220037233 rs115173026 Human genes 0.000 description 1
- 239000003352 sequestering agent Substances 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- PGAYKUDHDPZSLB-UHFFFAOYSA-M sodium octadecanoate oxirane Chemical compound C(CCCCCCCCCCCCCCCCC)(=O)[O-].[Na+].C1CO1 PGAYKUDHDPZSLB-UHFFFAOYSA-M 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
Definitions
- the present invention relates to an enzymatic detergent and bleaching composition
- an enzymatic detergent and bleaching composition comprising as essential ingredients a lipolytic enzyme and a bleaching system.
- Enzymatic detergent and bleaching compositions are well known in the art. They normally comprise proteolytic and/or amylolytic enzymes and a bleaching system usually consisting of sodium perborate, either as such or in admixture with a low temperature bleach activator, e.g. tetraacetyl ethylene diamine (TAED).
- TAED tetraacetyl ethylene diamine
- pancreatic lipase and Rhizopus lipase were both unstable in detergent solutions which contained a mixture of an anionic and a nonionic synthetic detergent, pentasodium triphosphate and sodium perborate, whereas these lipases were far less unstable in solutions with sodium perborate alone.
- lipases which are especially suitable for inclusion in detergent compositions. These lipases are significantly less affected by a bleaching system than other lipases. These bleaching systems comprise sodium perborate and TAED.
- the class of lipases of the present invention consists of fungal lipases producible by Humicola lanuginosa, Thermomyces lanuginosus and bacterial lipases which show a positive immunological cross-reaction with the antibody of the lipase produced by the micro-organism Chromobacter viscosum var. lipolyticum NRRL B-3673.
- This micro-organism has been described in Dutch patent specification 154 269 of Toyo Jozo Kabushiki Kaisha and has been deposited with the Fermentation Research Institute, Agency of Industrial Science and Technology, Ministry of International Trade & Industry, Tokyo, Japan, and added to the permanent culture collection under nr.
- TJ lipase The lipase produced by this micro-organism is commercially available from Toyo Jozo Co, Tagata, Japan, hereafter referred to as "TJ lipase".
- TJ lipase These bacterial lipases of the present invention should show a positive immunological cross-reaction with the TJ lipase antibody, using the standard and well-known immunodiffusion procedure according to Ouchterlony (Acta. Med. Scan., 133, pages 76-79 (1950)).
- the preparation of the antiserum is carried out as follows:
- Equal volumes of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an emulsion is obtained.
- Two female rabbits are injected with 2 ml samples of the emulsion according to the following scheme:
- the serum containing the required antibody is prepared by centrifugation of clotted blood, taken on day 67.
- the titre of the anti-TJ-lipase antiserum is determined by the inspection of precipitation of serial dilutions of antigen and antiserum according to Ouchterlony procedure. A 2 5 dilution of antiserum was the dilution that still gave a visible precipitation with an antigen concentration of 0.1 mg/ml.
- lipases showing a positive immunological cross-reaction with the TJ-lipase antibody as hereabove described are lipases according to the present invention.
- Typical examples thereof are the lipase ex Pseudomonas fluorescens IAM 1057 available from Amano Pharmaceutical Co, Nagoya, Japan, under the trade-name Amano-P lipase, the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade-name Amano-B), lipase ex Pseudomonas nitroreducens var. lipolyticum FERM P-1338, the lipase ex Pseudomonas sp.
- Chromobacter viscosum e.g. Chromobacter viscosum var. lipolyticum NRRL B-3673, commercially available from Toyo Jozo Co., Tagata, Japan; and further Chromobacter viscosum lipases from US Biochemical Corp., USA and Diosynth Co., The Netherlands, and lipases ex Pseudomonas gladioli.
- a fungal lipase as defined above is the lipase ex Humicola lanuginosa, available from Amano under the trade-name Amano-CE.
- the lipases of the present invention are included in the detergent and bleaching composition in such an amount that the final composition has a lipolytic enzyme activity of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition.
- lipases can be used in their non-purified form or in a purified form, e.g. purified with the aid of well-known adsorption methods, such as phenyl sepharose adsorption techniques.
- the bacterial cross-reacting lipases are preferred in view of their better overall performance.
- the bleaching system used according to the present invention is stronger than the sodium perborate/TAED system. This latter system, through a perhydrolysis reaction, forms a peroxyacid, i.e. peracetic acid, but at a rather low rate.
- the bleaching systems according to the present invention must be stronger than this sodium perborate/TAED system, by which is to be understood that the system either is based on a peracid (inorganic or organic) which is stronger than the peracetic acid or yields, on perhydrolysis, an organic peracid, including peracetic acid, faster than the sodium perborate/TAED system.
- the bleaching system may consist of a bleaching agent as such or may consist of a bleaching agent together with a bleach precursor.
- a bleaching agent as such alkali metal monopersulphates, furthermore organic peracids such as diperoxy dodecanedioic acid, diperoxy tetradecanedioic acid, diperoxyhexadecane dioic acid, mono- and diperazelaic acid, mono- and diperbrassylic acid, monoperoxy phthalic acid, perbenzoic acid, can be used, either as acid or in the form of their salts.
- this system comprises a bleaching agent which reacts with a bleach precursor to form a peracid in solution faster than the sodium perborate/TAED system.
- a bleaching agent which reacts with a bleach precursor to form a peracid in solution faster than the sodium perborate/TAED system.
- faster is meant that the precursor will have a rate of peroxy acid release of at least 2 (two) times, preferably at least 5 (five) times faster than TAED under the same conditions.
- Typical examples of such systems are sodium perborate with sodium nonanoyloxy benzene sulphonate or sodium trimethyl hexanoyloxy benzene sulphonate or sodium acetoxy benzene sulphonate or sodium benzoyloxy benzene sulphonate.
- the preferred systems of the present invention are sodium perborate with sodium nonanoyloxy benzene sulphonate, diperoxy dodecane dioic acid or monopersulphate.
- the amount of the bleaching system in the composition varies from 1-50%, usually from 5-40% by weight.
- the molar ratio of the bleach precursor to the percompound such as sodium perborate varies from 1:1 to 1:35, preferably from 1:2 to 1:20. Mixtures of various bleaching agents and various bleach precursors in accordance with the invention can also be used.
- compositions of the present invention may furthermore contain one or more detergent active materials, such as soaps, anionic, nonionic, cationic and zwitterionic synthetic detergents or mixtures thereof.
- detergent active materials such as soaps, anionic, nonionic, cationic and zwitterionic synthetic detergents or mixtures thereof.
- amount of detergent active material present in the composition will range from 1-50%, preferably 2-40% and particularly preferably 5-30% by weight.
- Suitable examples of detergent active materials can be found in Schwartz, Perry and Berch “Surface Active Agents and Detergents", Vol. I (1949) and Vol. II (1958) and M. Schick "Nonionic Surfactants” Vol. I (1967).
- compositions may furthermore include the usual detergent ingredients in the usual amounts. They may be unbuilt or built, and may be of the zero-P type (i.e. not containing phosphorus-containing builders). Thus, the compositions may contain from 1-60%, preferably from 5-30% by weight of one or more organic and/or inorganic builders. Typical examples of such builders are the alkali metal ortho-, pyro- and tripolyphosphates, alkali metal carbonates, either alone or in admixture with calcite, alkali metal citrates, alkali metal nitrilotriacetates, carboxymethyloxy succinates, zeolites, polyacetal carboxylates and so on.
- compositions may furthermore comprise lather boosters, foam depressors, anti-corrosion agents, soil-suspending agents, sequestering agents, anti-soil redeposition agents, perfumes, dyes, stabilizing agents for the enzymes and bleaching agents and so on.
- They may also comprise enzymes other than lipases, such as proteases, amylases, oxidases and cellulases.
- proteases are often affected by strong bleaches, in the present invention, when used together with the lipases of the present invention, the overall performance of the enzyme system is often not significantly affected.
- the compositions may comprise such other enzymes in an amount of 0.01-10% by weight.
- the amount, expressed in proteolytic activity is usually from 0.1-50 GU/ mg based on the final composition.
- a GU is a glycine unit, which is the amount of proteolytic enzyme which under standard incubation conditions produces an amount of terminal NH 2 -groups equivalent to 1 microgramme/ml of glycine.
- compositions of the present invention can be formulated in any desired form, such as powders, bars, pastes, liquids, etc.
- the invention will further be illustrated by way of Example.
- the lipase stability is measured by determining the residual lipase activity with the pH-stat. method.
- Dequest 2041 ethylene diamine tetra(methylene phosphonic acid)
- TAED tetraacetyl ethylene diamine
- SNOBS sodium nonaoyloxy benzene sulphonate
- the residual percentage of fatty material on the test cloths was determined and the reflectance was measured in a Reflectometer at 460 mm with a UV filter in the light pathway.
- the residual fatty material was measured by extracting the dried test cloths with petroleum ether, distilling off the solvent and weighing the resulting fatty matter
- Examples 1 and 2 were repeated, but now in the presence of 20 GU (glycine unit)/ ml Savinase®, a proteolytic enzyme ex NOVO.
- This composition was used in a concentration of 4.28 g/l.
- the washing was carried out as follows: Washing for 5 minutes at 30° C., thereafter adding citric acid to a pH of 8.5-9.0 and subsequently washing for 25 minutes at 30° C.
- Multi-wash monitor cotton test cloth soiled with a mixture of inorganic pigments, groundnut oil and milk powder (test cloth A) or a mixture of inorganic pigments, palm oil and protein (cocktail 2) (test cloth B).
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Abstract
The invention relates to the use of a certain class of lipases together with strong bleaching agents in detergent compositions. This class of lipases consists of fungal lipases ex Humicola lanuginosa or Thermomyces lanuginosus, and bacterial lipases which show a positive immunological cross-reaction with the antibody of the lipase produced by Chromobacter viscosum var. lipolyticum NRRL B-3673. The strong bleaching agents are stronger than the sodium perborate/TAED system, i.e. stronger than peracetic acid or they yield, on perhydrolysis, a peracid faster than the sodium perborate/TAED system.
Description
The present invention relates to an enzymatic detergent and bleaching composition comprising as essential ingredients a lipolytic enzyme and a bleaching system.
Enzymatic detergent and bleaching compositions are well known in the art. They normally comprise proteolytic and/or amylolytic enzymes and a bleaching system usually consisting of sodium perborate, either as such or in admixture with a low temperature bleach activator, e.g. tetraacetyl ethylene diamine (TAED). Although lipolytic enzymes have been mentioned in the prior art as possible enzymes for inclusion in detergent compositions, there is relatively little prior art specifically concerned with lipases for inclusion in detergent and bleaching compositions.
In a rather recent article in the "Journal of Applied Biochemistry", 2 (1980), pages 218-229, Andree et al. have reported their investigations of lipases as detergent components. They found that pancreatic lipase and Rhizopus lipase were both unstable in detergent solutions which contained a mixture of an anionic and a nonionic synthetic detergent, pentasodium triphosphate and sodium perborate, whereas these lipases were far less unstable in solutions with sodium perborate alone.
In the prior art, as far as we are aware, there is no clear teaching about the compatibility or incompatibility of lipases and bleaching systems, and consequently one cannot predict which lipases would be compatible with which bleaching systems.
In our co-pending patent application No. 8514707, filed in Great Britain on 11 June 1985 we identified a certain class of lipases which are especially suitable for inclusion in detergent compositions. These lipases are significantly less affected by a bleaching system than other lipases. These bleaching systems comprise sodium perborate and TAED.
We have now surprisingly found that a certain class of lipases, which will be defined hereafter, is quite compatible with bleaching systems which are stronger than the sodium perborate/TAED system, such systems being defined in more detail hereafter. Whereas, as stated above, there is no general rule to be found in the prior art concerning which lipases would be compatible with which bleach systems, we have discovered that each member of the class of lipases according to our invention is compatible with bleaching systems which are stronger than the sodium perborate/TAED system. The class of lipases of the present invention consists of fungal lipases producible by Humicola lanuginosa, Thermomyces lanuginosus and bacterial lipases which show a positive immunological cross-reaction with the antibody of the lipase produced by the micro-organism Chromobacter viscosum var. lipolyticum NRRL B-3673. This micro-organism has been described in Dutch patent specification 154 269 of Toyo Jozo Kabushiki Kaisha and has been deposited with the Fermentation Research Institute, Agency of Industrial Science and Technology, Ministry of International Trade & Industry, Tokyo, Japan, and added to the permanent culture collection under nr. Ko Hatsu Ken Kin Ki 137 and is available to the public at the United States Department of Agriculture, Agricultural Research Service, Northern Utilization and Development Division at Peoria, Ill., USA, under the nr. NRRL B-3673. The lipase produced by this micro-organism is commercially available from Toyo Jozo Co, Tagata, Japan, hereafter referred to as "TJ lipase". These bacterial lipases of the present invention should show a positive immunological cross-reaction with the TJ lipase antibody, using the standard and well-known immunodiffusion procedure according to Ouchterlony (Acta. Med. Scan., 133, pages 76-79 (1950)).
The preparation of the antiserum is carried out as follows:
Equal volumes of 0.1 mg/ml antigen and of Freund's adjuvant (complete or incomplete) are mixed until an emulsion is obtained. Two female rabbits are injected with 2 ml samples of the emulsion according to the following scheme:
day 0: antigen in complete Freund's adjuvant
day 4: antigen in complete Freund's adjuvant
day 32: antigen in incomplete Freund's adjuvant
day 60: booster of antigen in incomplete Freund's adjuvant
The serum containing the required antibody is prepared by centrifugation of clotted blood, taken on day 67.
The titre of the anti-TJ-lipase antiserum is determined by the inspection of precipitation of serial dilutions of antigen and antiserum according to Ouchterlony procedure. A 25 dilution of antiserum was the dilution that still gave a visible precipitation with an antigen concentration of 0.1 mg/ml.
All lipases showing a positive immunological cross-reaction with the TJ-lipase antibody as hereabove described are lipases according to the present invention. Typical examples thereof are the lipase ex Pseudomonas fluorescens IAM 1057 available from Amano Pharmaceutical Co, Nagoya, Japan, under the trade-name Amano-P lipase, the lipase ex Pseudomonas fragi FERM P 1339 (available under the trade-name Amano-B), lipase ex Pseudomonas nitroreducens var. lipolyticum FERM P-1338, the lipase ex Pseudomonas sp. available under the trade-name Amano CES, the lipase ex Pseudomonas cepacia, lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var. lipolyticum NRRL B-3673, commercially available from Toyo Jozo Co., Tagata, Japan; and further Chromobacter viscosum lipases from US Biochemical Corp., USA and Diosynth Co., The Netherlands, and lipases ex Pseudomonas gladioli.
An example of a fungal lipase as defined above is the lipase ex Humicola lanuginosa, available from Amano under the trade-name Amano-CE.
The lipases of the present invention are included in the detergent and bleaching composition in such an amount that the final composition has a lipolytic enzyme activity of from 100 to 0.005 LU/mg, preferably 25 to 0.05 LU/mg of the composition.
A Lipase Unit (LU) is that amount of lipase which produces 1 μmol of titratable fatty acid per minute in a pH stat. under the following conditions: temperature 30° C.; pH=9.0; substrate is an emulsion of 3.3 wt.% of olive oil and 3.3% gum arabic, in the presence of 13 mmol/l Ca2+ and 20 mol/l NaCl in 5 mmol/l Tris-buffer.
Naturally, mixtures of the above lipases can be used. The lipases can be used in their non-purified form or in a purified form, e.g. purified with the aid of well-known adsorption methods, such as phenyl sepharose adsorption techniques.
Of the lipases according to the present invention, the bacterial cross-reacting lipases are preferred in view of their better overall performance. The bleaching system used according to the present invention is stronger than the sodium perborate/TAED system. This latter system, through a perhydrolysis reaction, forms a peroxyacid, i.e. peracetic acid, but at a rather low rate. The bleaching systems according to the present invention must be stronger than this sodium perborate/TAED system, by which is to be understood that the system either is based on a peracid (inorganic or organic) which is stronger than the peracetic acid or yields, on perhydrolysis, an organic peracid, including peracetic acid, faster than the sodium perborate/TAED system. The bleaching system may consist of a bleaching agent as such or may consist of a bleaching agent together with a bleach precursor. As bleaching agent as such alkali metal monopersulphates, furthermore organic peracids such as diperoxy dodecanedioic acid, diperoxy tetradecanedioic acid, diperoxyhexadecane dioic acid, mono- and diperazelaic acid, mono- and diperbrassylic acid, monoperoxy phthalic acid, perbenzoic acid, can be used, either as acid or in the form of their salts.
When a system comprising a bleach precursor is used, this system comprises a bleaching agent which reacts with a bleach precursor to form a peracid in solution faster than the sodium perborate/TAED system. By faster is meant that the precursor will have a rate of peroxy acid release of at least 2 (two) times, preferably at least 5 (five) times faster than TAED under the same conditions.
Typical examples of such systems are sodium perborate with sodium nonanoyloxy benzene sulphonate or sodium trimethyl hexanoyloxy benzene sulphonate or sodium acetoxy benzene sulphonate or sodium benzoyloxy benzene sulphonate.
The preferred systems of the present invention are sodium perborate with sodium nonanoyloxy benzene sulphonate, diperoxy dodecane dioic acid or monopersulphate.
In general, the amount of the bleaching system in the composition varies from 1-50%, usually from 5-40% by weight. When a bleach precursor is present, the molar ratio of the bleach precursor to the percompound such as sodium perborate varies from 1:1 to 1:35, preferably from 1:2 to 1:20. Mixtures of various bleaching agents and various bleach precursors in accordance with the invention can also be used.
The compositions of the present invention may furthermore contain one or more detergent active materials, such as soaps, anionic, nonionic, cationic and zwitterionic synthetic detergents or mixtures thereof. Usually the amount of detergent active material present in the composition will range from 1-50%, preferably 2-40% and particularly preferably 5-30% by weight. Suitable examples of detergent active materials can be found in Schwartz, Perry and Berch "Surface Active Agents and Detergents", Vol. I (1949) and Vol. II (1958) and M. Schick "Nonionic Surfactants" Vol. I (1967).
The compositions may furthermore include the usual detergent ingredients in the usual amounts. They may be unbuilt or built, and may be of the zero-P type (i.e. not containing phosphorus-containing builders). Thus, the compositions may contain from 1-60%, preferably from 5-30% by weight of one or more organic and/or inorganic builders. Typical examples of such builders are the alkali metal ortho-, pyro- and tripolyphosphates, alkali metal carbonates, either alone or in admixture with calcite, alkali metal citrates, alkali metal nitrilotriacetates, carboxymethyloxy succinates, zeolites, polyacetal carboxylates and so on.
The compositions may furthermore comprise lather boosters, foam depressors, anti-corrosion agents, soil-suspending agents, sequestering agents, anti-soil redeposition agents, perfumes, dyes, stabilizing agents for the enzymes and bleaching agents and so on. They may also comprise enzymes other than lipases, such as proteases, amylases, oxidases and cellulases. In this respect it has been found that, whereas proteases are often affected by strong bleaches, in the present invention, when used together with the lipases of the present invention, the overall performance of the enzyme system is often not significantly affected. In general, the compositions may comprise such other enzymes in an amount of 0.01-10% by weight. For proteases, the amount, expressed in proteolytic activity, is usually from 0.1-50 GU/mg based on the final composition.
A GU is a glycine unit, which is the amount of proteolytic enzyme which under standard incubation conditions produces an amount of terminal NH2 -groups equivalent to 1 microgramme/ml of glycine.
The compositions of the present invention can be formulated in any desired form, such as powders, bars, pastes, liquids, etc.
The invention will further be illustrated by way of Example.
The stability of various lipases in the presence of a bleaching system was measured as follows:
To a solution of 4 g/l of a detergent composition* and 0.03 g/l Dequest 2041 in water with a hardness of 30° FH and a temperature of 30° C., an amount of lipase is added to obtain 15-20 lipase units/ml.
______________________________________
% by weight
______________________________________
Sodium dodecyl benzene sulphonate
6.5
C.sub.14 -C.sub.15 primary alcohol, condensed
2.0
with 11 moles of ethylene oxide
Sodium stearate 1.0
Sodium silicate 7.0
Sodium carboxymethyl cellulose
0.5
Na.sub.2 SO.sub.4 37.0
Pentasodium triphosphate
15.0
Trisodium orthophosphate
5.0
Fluorescer 0.2
Ethylene diamine tetraacetic acid
0.5
Water 6.2
Dyes 0.01
______________________________________
The pH is adjusted with NaOH to pH 10.0 at 30° C. At t=0 a bleach system is added:
(a) 292 mg/l TAED (65% pure) and 700 mg/l sodium perborate monohydrate or
(b) 1880 mg/l DPDA (12% pure) or
(c) 822 mg/l SNOBS (80% pure) and 1500 mg/l sodium perborate monohydrate or
(d) 506 mg/l MPS (in the form of the commercial product Caroate®) or
(e) 475 mg/l P15 (95% pure) and 700 mg/l sodium perborate monohydrate.
This yields 1.5 mmolar peracid in solution for all bleach systems. The lipase stability is measured by determining the residual lipase activity with the pH-stat. method.
Dequest 2041=ethylene diamine tetra(methylene phosphonic acid)
TAED=tetraacetyl ethylene diamine
DPDA=diperoxy dodecanedioic acid
SNOBS=sodium nonaoyloxy benzene sulphonate
MPS=sodium monopersulphate
P15=sodium benzoyloxy benzene sulphonate
The following results were obtained: No bleach TAED/perb. SNOBS/perb. DPDA MPS P15 activity.sup.(1) activity.sup.(1) activity.sup.(1) activity. sup.(1) activity.sup.(1) activity.sup.(1) 10 30 t1/2 10 30 t1/2 10 30 t1/2 10 30 t1/2 10 30 t1/2 10 30 t1/2 Lipase ex. Trade-name min min (min) min min (min) min min (min) min min (min) min min (min) min min (min) Humicola Amano CE 92 93 * 92 95 * 82 80 * 95 94 * 96 82 * 90 83 * lanuginosa Thermomyces -- 96 99 * 98 98 * 81 79 * 95 90 * 82 78 * 85 80 * lanuginosus Pseudomonas -- 97 97 * 97 92 * 90 80 * 100 99 * 89 80 * 92 77 * gladioli Chromobacter Diosynth 105 99 * 95 93 * 95 80 * 100 103 * 100 96 * 100 90 * viscosum Chromobacter Toyo Jozo 100 95 * 100 86 * 80 58 * 107 98 * 85 62 * 93 63 * viscosum Pseudomonas Amano P 100 98 * 92 100 * 85 80 * 109 100 * 89 85 * 102 83 * fluorescens Pseudomonas ex NOVO 93 90 * 98 94 * 89 81 * 100 98 * 97 96 * 95 84 * cepacia Pseudomonas Amano B 101 122 * 73 66 * 125 125 * 91 95 * 125 125 * 91 88 * fragi Pseudomonas Amano CES 92 89 * 102 93 * 79 67 * 101 96 * 104 95 * 104 97 * fluorescens Aspergillus Amano AP 6 110 90 * 100 64 43 14 <5 2 62 <5 12 78 40 24 30 9 7 niger Mucor Miehei SP 225 67 46 28 95 58 35 81 46 28 86 68 * 13 <5 4 73 44 26 Fusarium SP 285 23 < 5 4 23 <5 3 30 <5 4 24 <5 3 25 <5 5 23 <5 4 oxysporum Mucor Esterase 64 21 15 67 25 16 59 24 12 50 20 10 10 <5 4 60 20 12 miehei MM Alcaligenes Lipase PL 55 29 13 40 23 7 33 10 6 nd. nd. nd. species (batch 1) Candida Lipase MY <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 cyclindracea Candida Lipase MY <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 cyclindracea Rhizopus Saiken A <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 species A 300 Alcaligenes Lipase PL 27 13 4 18 11 4 <5 <5 2 18 15 5 17 13 5 17 7 4 species ex Meito ATCC 31371) (batch 2) Porcine L-3126 15 <5 1 5 <5 1 <5 <5 1 13 <5 1 <5 <5 1 <5 <5 1 pancreas Sigma Rhizopus 580,000 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 arrhizus Rapidase Mucor M-AP 31 <5 7 21 <5 6 27 <5 7 90 49 30 16 <5 4 36 <5 8 javanicus Amano Candida ENZECO <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 rugosa lipase 30,000 Rhizopus Lipase 2A <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 species Nagase Rhizopus Lipase 2B <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 species Nagase Candida OF 360 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 cylindracea Meito Kogyo Candida L-1754 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 cylindracea Sigma Rhizopus F-AP <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 javanicus Amano Rhizopus N <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 <5 <5 <1 niveus Amano *too large to determine from these experiments .sup.(1) residual lipase activity (% of input) t1/2 = half life time
Various lipases were tested in washing experiments under the following conditions:
______________________________________
lipase concentration
15 LU/ml
detergent composition
as in Example 1
dosage 4 g/l
bleach systems sodium perborate + SNOBS
sodium perborate + TAED
DPDA
MPS
All generating 1.5 mmol
peracid in solution
temperature heat-up to 30° C.; 40 min in
total
water hardness 39° F.H
cloth/liquor ratio
1.8
number of soil/wash
3
cycles
cloths polyester soiled with mustard
or sateh sauce
PCBC 1
______________________________________
After these soil/wash cycles, the residual percentage of fatty material on the test cloths was determined and the reflectance was measured in a Reflectometer at 460 mm with a UV filter in the light pathway. The residual fatty material was measured by extracting the dried test cloths with petroleum ether, distilling off the solvent and weighing the resulting fatty matter
The following results were obtained:
______________________________________
Cloth Sateh sauce Mustard
Lipase TJ AP AP6 MY NO TJ AP AP6 MY NO
______________________________________
SNOBS 3.0 2.9 7.6 6.4 6.7 1.6 1.3
2.4 2.4 2.6
TAED 3.2 3.1 7.2 6.7 6.5 1.7 1.4
2.3 2.4 2.5
DPDA 2.8 2.8 7.3 6.3 6.4 1.6 1.5
2.3 2.3 2.4
MPS 4.2 2.8 7.2 6.7 6.6 1.9 1.4
2.3 2.5 2.4
NO 3.4 2.8 7.2 6.7 6.7 1.6 1.4
2.4 2.5 2.4
bleach
______________________________________
TJ = Lipase ex Chromobacter viscosum, made by Toyo Jozo
AP = Amano P lipase
AP6 = Amano AP6 lipase
MY = Meito Sangyo lipase
NO = No lipase used
______________________________________
Lipase
Cloth Bleach TJ AP NO
______________________________________
Sateh SNOBS 73.3 73.8 69.2
sauce TAED 68.5 69.3 65.7
NO bleach 65.7 65.5 61.9
Mustard SNOBS 70.8 70.3 67.2
TAED 64.7 65.3 62.8
NO bleach 61.4 63.2 60.0
PCBCl SNOBS 36.5 36.2 36.2
TAED 34.3 33.7 33.5
NO bleach 27.0 26.8 26.2
______________________________________
Examples 1 and 2 were repeated, but now in the presence of 20 GU (glycine unit)/ml Savinase®, a proteolytic enzyme ex NOVO.
The following results were obtained:
__________________________________________________________________________
No bleach TAED/perb. SNOBS/perb.
activity.sup.(1)
activity.sup.(1)
activity.sup.(1)
10 30 t1/2
10 30 t1/2
10 30 t1/2
Lipase min
min
(min)
min
min (min)
min
min
(min)
__________________________________________________________________________
Ps. gladioli
81 56 37 76 51 31 76 55 36
Amano P 51 17 10 56 20 12 40 16 6
Diosynth
77 45 27 83 53 35 81 62 >40
Amano CE
94 92 * 89 71 * 64 61 *
Amano B 82 71 * 63 59 * 95 83 *
Amano CES
44 12 8 40 13 8 46 26 9
Th. 89 90 * 88 86 * 93 90 *
lanuginosus
Ps. cepacia
65 35 18 72 38 19 65 34 19
Toyo Jozo
79 48 30 71 38 18 72 47 28
Amano AP6
96 83 * 82 38 25 <5 <5 3
Esterase MM
64 21 13 38 15 8 43 12 8
Novo SP285
18 <5 4 16 <5 4 16 <5 4
Novo SP225
106
85 * 94 68 * 94 68 *
PL (batch 2)
28 11 5 20 8 5 11 <5 3
L-3126 21 <5 1 6 <5 1 <5 <5 1
S80,000 <5 <5 <1 <5 <5 <1 <5 <5 <1
M-AP 24 <5 6 18 <5 6 29 <5 7
ENZECO <5 <5 <1 <5 <5 <1 <5 <5 <1
Lipase 2A
<5 <5 <1 <5 <5 <1 <5 <5 <1
Lipase 2B
<5 <5 <1 <5 <5 <1 <5 <5 <1
OF 360 <5 <5 <1 <5 <5 <1 <5 <5 <1
L-1754 <5 <5 <1 <5 <5 <1 <5 <5 <1
F-AP <5 <5 <1 <5 <5 <1 <5 <5 <1
MY <5 <5 <1 <5 <5 <1 <5 <5 <1
Candida
<5 <5 <1 <5 <5 <1 <5 <5 <1
cyl.
N <5 <5 <1 <5 <5 <1 <5 <5 <1
__________________________________________________________________________
DPDA MPS P15
activity.sup.(1)
activity.sup.(1)
activity.sup.(1)
10 30 t1/2
10 30 t1/2
10 30 t1/2
Lipase min
min
(min)
min
min (min)
min
min
(min)
__________________________________________________________________________
Ps. gladioli
90 70 >60 63 47 20 81 42 26
Amano P 60 24 12 43 27 8 55 15 11
Diosynth
78 62 >40 67 52 32 78 32 19
Amano CE
86 91 * 100
92 * 87 82 *
Amano B 100
86 * 97 66 * 93 85 *
Amano CES
57 32 14 89 76 * 43 20 8
Th. 95 90 * 91 75 * 87 81 *
lanuginosus
Ps. cepacia
59 42 18 54 32 12 65 28 17
Toyo Jozo
82 52 33 38 22 8 74 29 17
Amano AP6
61 15 12 91 79 * 55 24 11
Esterase MM
68 25 16 10 <5 5 74 25 17
Novo SP285
24 <5 5 16 <5 4 20 <5 4
Novo SP225
97 73 * 30 8 7 88 51 30
PL (batch 2)
20 <5 5 14 <5 5 23 9 4
L-3126 13 <5 <1 7 <5 <1 7 <5 <1
S80,000 <5 <5 <1 <5 <5 <1 <5 <5 <1
M-AP 87 53 33 14 <5 4 30 <5 8
ENZECO <5 <5 <1 <5 <5 <1 <5 <5 <1
Lipase 2A
<5 <5 <1 <5 <5 <1 <5 <5 <1
Lipase 2B
<5 <5 <1 <5 <5 <1 <5 <5 <1
OF 360 <5 <5 <1 <5 <5 <1 <5 <5 <1
L-1754 <5 <5 <1 <5 <5 <1 <5 <5 < 1
F-AP <5 <5 <1 <5 <5 <1 <5 <5 <1
MY <5 <5 <1 <5 <5 <1 <5 <5 <1
Candida <5 <5 <1 <5 <5 <1 <5 <5 <1
cyl.
N <5 <5 <1 <5 <5 <1 <5 <5 <1
__________________________________________________________________________
*too large to determine from these experiments
.sup.(1) residual lipase activity (% of input)
t1/2 = half time life
______________________________________
Lipase
Cloth Bleach TJ AP NO lipase
______________________________________
Sateh SNOBS 74.0 75.5 72.3
sauce TAED 71.2 71.9 69.0
NO bleach 65.6 66.2 64.8
Mustard SNOBS 74.3 73.6 72.5
TAED 70.6 69.8 68.6
NO bleach 66.8 65.6 65.1
PCBCl SNOBS 36.9 36.9 36.5
TAED 34.4 34.8 33.9
NO bleach 27.0 26.6 26.8
______________________________________
______________________________________
Lipase
Cloth Bleach TJ AP NO lipase
______________________________________
Sateh SNOBS 3.9 3.1 7.0
sauce TAED 4.1 3.4 7.0
DPDA 3.6 3.0 7.0
MPS 6.0 2.9 7.0
NO bleach 4.0 3.6 7.0
Mustard SNOBS 1.8 1.2 2.2.
TAED 1.8 1.3 2.2
DPDA 1.6 1.2 2.2
MPS 1.9 1.2 2.2
NO bleach 1.5 1.3 2.2
______________________________________
Wash and bleach tests were carried out using the following formulation:
______________________________________
% by weight
______________________________________
Sodium dodecyl benzene sulphonate
8.5
C.sub.12 -C.sub.15 primary alcohol, condensed
4.0
with 7 moles of ethylene oxide
Sodium-hardened rapeseed oil soap
1.5
Sodium triphosphate 33.0
Sodium carbonate 5.0
Sodium silicate 6.0
Sodium sulphate 20.0
Water 9.0
Fluorescers, soil-suspending agents,
minor amount
dyes, perfumes
Anti-foam granules 1.2
Dequest ® 2047 (34% pure)
0.3
______________________________________
This composition was used in a concentration of 4.28 g/l. The washing was carried out as follows: Washing for 5 minutes at 30° C., thereafter adding citric acid to a pH of 8.5-9.0 and subsequently washing for 25 minutes at 30° C.
The same washing tests were carried out with the above formulation (4.28 g/l), to which 0.292 g/l TAED (65% pure) and 0.7 g/l sodium perborate monohydrate were added (yielding 1.5 mmol peracid in solution), or to which 1.88 g/l DPDA (12% pure) was added (yielding 1.5 mmol peracid in solution).
Test cloths:
Single wash monitor: BCl.
Multi-wash monitor: cotton test cloth soiled with a mixture of inorganic pigments, groundnut oil and milk powder (test cloth A) or a mixture of inorganic pigments, palm oil and protein (cocktail 2) (test cloth B).
Results:
Bleach effect.sup.(1) (ΔR460*)
______________________________________
Bleach
BC-1
______________________________________
TAED 6.5
DPDA 8.9
NO -0.7
______________________________________
__________________________________________________________________________
Multi wash
Cloth
AS8/ANO/MP AS8/PO/C2
Lipase
Cepacia Cepacia
Bleach
SP341
Gladioli
Esterase MM
Saiken A300
NO SP 341
Gladioli
Esterase MM
Saiken A300
NO
__________________________________________________________________________
Residual fat* after fourth cycle
TAED
3.5 3.6 3.6 4.8 4.4
10.4 11.1 11.1 17.1 16.4
DPDA
3.8 3.8 3.7 4.3 5.1
10.6 9.7 10.1 15.7 17.9
NO 3.1 3.3 3.8 4.2 4.3
9.7 10.1 11.1 14.7 16.3
Relectance values after fourth cycle:
TAED
81.2 81.5 80.4 74.7 75.3
54.0 53.7 53.9 49.7 50.2
DPDA
83.4 83.4 83.0 78.9 75.9
53.9 54.1 53.0 50.6 49.2
NO 80.8 80.5 78.2 75.9 75.3
45.1 51.3 44.0 42.8 38.3
__________________________________________________________________________
The performance of Cepacia lipase and lipase from Mucor miehei (SP225 ex NOVO) in the presence of TAED/perborate and P15/perborate was tested on test cloths in washing machines using the composition of Example 4 (the base powder)+SavinaseR.
4° wash result of MCSW.
Monitors
single wash: AS10 (for protease performance) BCl (for bleach performance) EMPA 114 (for bleach performance)
multi wash: Cotton test cloths soiled with a mixture of inorganic pigments, palm oil and protein (cocktail 2)
Conditions
3.5 g/l base powder
30 min. 40° C.
40° FH
protease: 20 GU/ml Savinase
lipase: Cepacia lipase or SP225: 3 LU/ml
bleach: 428 mg/l P15 (70% pure)+467 mg/l perborate monohydrate or 195 mg/l TAED (65% pure)+467 mg/l perborate monohydrate giving 1.0 mmol peracid in solution
3.5 kg soiled load present.
The results on multi-wash monitor were:
______________________________________
Residual fat data
(% F.M.) Reflectance of test cloth
Lipase (ΔR460*)
Cepa- Lipase
Bleach
cia SP225 NO Bleach
Cepacia
SP225 NO
______________________________________
TAED 9.5 11.9 12.4 TAED 71.8 68.8 67.8
P15 11.0 13.0 14.4 P15 69.8 67.6 65.0
NO -- -- 14.0 NO -- -- 59.1
______________________________________
Lipase effect on multi-wash monitor
______________________________________
Fat removal Reflectance benefit
(Δ% F.M.) (ΔR460*)
Lipase Lipase
Bleach
Cepacia SP225 Bleach Cepacia SP225
______________________________________
TAED 2.9 0.5 TAED 4.0 1.0
P15 3.4 1.4 P15 4.8 2.6
______________________________________
Bleach effect 1○ (ΔR460*) Protease effect 1○ (ΔR460*)
______________________________________
Bleach BC-1 EMPA 114 Protease
AS 10
______________________________________
TAED 6.6 23.2 Savinase
34.8
P15 12.9 28.3 NO 9.8
NO 0.5 14.4
______________________________________
Claims (6)
1. A detergent composition comprising from 1-50% by weight of one or more detergent-active materials, from 0-60% by weight of a builder, from 1-50% by weight of a bleaching agent and lipolytic enzymes in an amount of 0.005-100 lipolytic units per milligram of the composition, wherein the bleaching agent is based on an inorganic or organic peracid or salt thereof which is stronger than peracetic acid or comprises a bleaching agent and a bleach precursor which yields, on perhydrolysis, a peracid faster than the system sodium perborate+tetraacetyl ethylene diamine, and the lipolytic enzyme is a fungal lipase obtained from Humicola lanuginosa or Thermomyces lanuginosus.
2. A composition according to claim 1, wherein the bleaching agent is an alkali metal persulphate.
3. A composition according to claim 1, wherein the bleaching agent is selected from the group consisting of diperoxy dodecanedioic acid, diperoxy tetradecanedioic acid, diperoxyhexadecane dioic acid, mono- and diperazelaic acid, mono- and diperbrassylic acid, monoperoxy phthalic acid, perbenzoic acid, and their salts.
4. A composition according to claim 1, wherein the bleaching agent comprises a bleaching agent and a bleach precursor which forms a peracid in solution at least two times faster than tetraacetyl ethylene diamine under the same conditions.
5. A composition according to claim 4, wherein the bleaching agent comprises sodium perborate and a bleach precursor selected from the group consisting of sodium nonanoyloxy benzene sulphonate, sodium trimethyl hexanoyloxy benzene sulphonate, sodium acetoxy benzene sulphonate and sodium benzoyloxy benzene sulphonate.
6. A composition according to any one of claims 1-5, wherein it further contains a proteolytic enzyme in an amount of 0.1-50 GU/mg of the composition.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB868629534A GB8629534D0 (en) | 1986-12-10 | 1986-12-10 | Enzymatic detergent & bleaching composition |
| GB8629534 | 1986-12-10 |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| US07/210,464 Continuation US4861509A (en) | 1986-12-10 | 1988-06-23 | Enzymatic detergent and bleaching composition |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| US4769173A true US4769173A (en) | 1988-09-06 |
Family
ID=10608784
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| US07/128,256 Expired - Lifetime US4769173A (en) | 1986-12-10 | 1987-12-03 | Enzymatic detergent and bleaching composition |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US4769173A (en) |
| EP (1) | EP0271152B1 (en) |
| JP (1) | JPH0696716B2 (en) |
| AU (1) | AU606101B2 (en) |
| BR (1) | BR8706681A (en) |
| CA (1) | CA1288366C (en) |
| DE (1) | DE3763813D1 (en) |
| ES (1) | ES2017710B3 (en) |
| GB (1) | GB8629534D0 (en) |
| ZA (1) | ZA879295B (en) |
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4861509A (en) * | 1986-12-10 | 1989-08-29 | Lever Brothers Company | Enzymatic detergent and bleaching composition |
| US4927559A (en) * | 1988-04-14 | 1990-05-22 | Lever Brothers Company | Low perborate to precursor ratio bleach systems |
| US4933287A (en) * | 1985-08-09 | 1990-06-12 | Gist-Brocades N.V. | Novel lipolytic enzymes and their use in detergent compositions |
| US5069809A (en) * | 1988-05-09 | 1991-12-03 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic detergent and bleaching composition containing a specific rdna technique cloned lipase |
| US5112518A (en) * | 1988-06-09 | 1992-05-12 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic dishwashing composition containing a chlorine-type bleaching agent |
| US5133893A (en) * | 1985-06-11 | 1992-07-28 | Lever Brothers Company | Enzymatic detergent composition |
| US5156761A (en) * | 1988-07-20 | 1992-10-20 | Dorrit Aaslyng | Method of stabilizing an enzymatic liquid detergent composition |
| US5211870A (en) * | 1992-03-11 | 1993-05-18 | The Procter & Gamble Company | Malodor-free cleansing bar composition containing zeolite odor controlling agent |
| US5707950A (en) * | 1994-11-18 | 1998-01-13 | The Procter & Gamble Company | Detergent compositions containing lipase and protease |
| US5837010A (en) * | 1994-11-18 | 1998-11-17 | Procter & Gamble Company | Detergent compositions containing a lipase variant at low levels |
| US5932532A (en) * | 1993-10-14 | 1999-08-03 | Procter & Gamble Company | Bleach compositions comprising protease enzyme |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8713756D0 (en) * | 1987-06-12 | 1987-07-15 | Procter & Gamble | Liquid detergent |
| US5292448A (en) * | 1988-05-10 | 1994-03-08 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic detergent composition |
| GB8813687D0 (en) * | 1988-06-09 | 1988-07-13 | Unilever Plc | Enzymatic dishwashing & rinsing composition |
| GB8815841D0 (en) * | 1988-07-04 | 1988-08-10 | Unilever Plc | Bleaching detergent compositions |
| GB8828955D0 (en) * | 1988-12-12 | 1989-01-25 | Unilever Plc | Enzyme-containing detergent compositions and their use |
| EP0619367A1 (en) * | 1993-04-06 | 1994-10-12 | The Procter & Gamble Company | Lavatory blocks containing enzymes |
| EP0622447A1 (en) * | 1993-04-26 | 1994-11-02 | The Procter & Gamble Company | Enzymatic detergent compositions inhibiting dye transfer |
| EP0817838B1 (en) * | 1995-03-30 | 2003-06-11 | Novozymes A/S | Alkaline lipolytic enzyme |
| US5919746A (en) * | 1995-03-30 | 1999-07-06 | Novo Nordisk A/S | Alkaline lipolytic enzyme |
| JPH09275977A (en) | 1996-04-18 | 1997-10-28 | Novo Nordisk As | New lipase and detergent composition |
| WO1998017790A1 (en) * | 1996-10-17 | 1998-04-30 | Novo Nordisk A/S | Lipase, process for producing the same, microorganism producing the same, and use of the lipase |
| CA2342066A1 (en) * | 1998-05-13 | 1999-11-18 | Dionisio Skepetaris | Stabilized disinfectant preparation containing peroxides |
| WO2014200656A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces umbrinus |
| WO2014200658A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from promicromonospora vindobonensis |
| WO2014200657A1 (en) | 2013-06-13 | 2014-12-18 | Danisco Us Inc. | Alpha-amylase from streptomyces xiamenensis |
| WO2014204596A1 (en) | 2013-06-17 | 2014-12-24 | Danisco Us Inc. | Alpha-amylase from bacillaceae family member |
| US20160186102A1 (en) | 2013-10-03 | 2016-06-30 | Danisco Us Inc. | Alpha-amylases from exiguobacterium, and methods of use, thereof |
| EP3060659B1 (en) | 2013-10-03 | 2019-05-29 | Danisco US Inc. | Alpha-amylases from exiguobacterium, and methods of use, thereof |
| US20160272957A1 (en) | 2013-11-20 | 2016-09-22 | Danisco Us Inc. | Variant alpha-amylases having reduced susceptibility to protease cleavage, and methods of use, thereof |
| WO2017173324A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
| WO2017173190A2 (en) | 2016-04-01 | 2017-10-05 | Danisco Us Inc. | Alpha-amylases, compositions & methods |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4011169A (en) * | 1973-06-29 | 1977-03-08 | The Procter & Gamble Company | Stabilization and enhancement of enzymatic activity |
| US4707291A (en) * | 1985-06-11 | 1987-11-17 | Lever Brothers Company | Enzymatic detergent composition |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BE790184A (en) * | 1971-10-18 | 1973-04-17 | Procter & Gamble Europ | |
| LU65030A1 (en) * | 1972-03-23 | 1973-09-26 | ||
| US4421664A (en) * | 1982-06-18 | 1983-12-20 | Economics Laboratory, Inc. | Compatible enzyme and oxidant bleaches containing cleaning composition |
| JPS5922999A (en) * | 1982-06-30 | 1984-02-06 | ザ・プロクタ−・エンド・ギヤンブル・カンパニ− | Bleaching composition |
| JPS6116998A (en) * | 1984-07-02 | 1986-01-24 | 花王株式会社 | Detergent composition |
| GB8514708D0 (en) * | 1985-06-11 | 1985-07-10 | Unilever Plc | Enzymatic detergent composition |
| JP2831639B2 (en) * | 1985-07-03 | 1998-12-02 | 花王株式会社 | Detergent composition |
| AU603101B2 (en) * | 1986-06-09 | 1990-11-08 | Clorox Company, The | Enzymatic perhydrolysis system and method of use for bleaching |
| JPS643456A (en) * | 1987-06-26 | 1989-01-09 | Hitachi Ltd | Thermal accumulative bath hot water feeder |
| JPS6434559A (en) * | 1987-07-30 | 1989-02-06 | Seiko Epson Corp | Structure for taking out cavity |
-
1986
- 1986-12-10 GB GB868629534A patent/GB8629534D0/en active Pending
-
1987
- 1987-12-02 EP EP87202384A patent/EP0271152B1/en not_active Expired - Lifetime
- 1987-12-02 ES ES87202384T patent/ES2017710B3/en not_active Expired - Lifetime
- 1987-12-02 DE DE8787202384T patent/DE3763813D1/en not_active Expired - Lifetime
- 1987-12-03 US US07/128,256 patent/US4769173A/en not_active Expired - Lifetime
- 1987-12-08 AU AU82222/87A patent/AU606101B2/en not_active Ceased
- 1987-12-08 CA CA000553754A patent/CA1288366C/en not_active Expired - Fee Related
- 1987-12-09 JP JP62311791A patent/JPH0696716B2/en not_active Expired - Lifetime
- 1987-12-09 BR BR8706681A patent/BR8706681A/en not_active IP Right Cessation
- 1987-12-10 ZA ZA879295A patent/ZA879295B/en unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4011169A (en) * | 1973-06-29 | 1977-03-08 | The Procter & Gamble Company | Stabilization and enhancement of enzymatic activity |
| US4707291A (en) * | 1985-06-11 | 1987-11-17 | Lever Brothers Company | Enzymatic detergent composition |
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5133893A (en) * | 1985-06-11 | 1992-07-28 | Lever Brothers Company | Enzymatic detergent composition |
| US4933287A (en) * | 1985-08-09 | 1990-06-12 | Gist-Brocades N.V. | Novel lipolytic enzymes and their use in detergent compositions |
| US4861509A (en) * | 1986-12-10 | 1989-08-29 | Lever Brothers Company | Enzymatic detergent and bleaching composition |
| US4927559A (en) * | 1988-04-14 | 1990-05-22 | Lever Brothers Company | Low perborate to precursor ratio bleach systems |
| US5069809A (en) * | 1988-05-09 | 1991-12-03 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic detergent and bleaching composition containing a specific rdna technique cloned lipase |
| US5112518A (en) * | 1988-06-09 | 1992-05-12 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic dishwashing composition containing a chlorine-type bleaching agent |
| US5156761A (en) * | 1988-07-20 | 1992-10-20 | Dorrit Aaslyng | Method of stabilizing an enzymatic liquid detergent composition |
| US5211870A (en) * | 1992-03-11 | 1993-05-18 | The Procter & Gamble Company | Malodor-free cleansing bar composition containing zeolite odor controlling agent |
| US5932532A (en) * | 1993-10-14 | 1999-08-03 | Procter & Gamble Company | Bleach compositions comprising protease enzyme |
| US5707950A (en) * | 1994-11-18 | 1998-01-13 | The Procter & Gamble Company | Detergent compositions containing lipase and protease |
| US5837010A (en) * | 1994-11-18 | 1998-11-17 | Procter & Gamble Company | Detergent compositions containing a lipase variant at low levels |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0696716B2 (en) | 1994-11-30 |
| EP0271152A3 (en) | 1988-08-10 |
| EP0271152A2 (en) | 1988-06-15 |
| ES2017710B3 (en) | 1991-03-01 |
| AU606101B2 (en) | 1991-01-31 |
| ZA879295B (en) | 1989-08-30 |
| AU8222287A (en) | 1988-06-16 |
| DE3763813D1 (en) | 1990-08-23 |
| CA1288366C (en) | 1991-09-03 |
| BR8706681A (en) | 1988-07-19 |
| EP0271152B1 (en) | 1990-07-18 |
| JPS63161087A (en) | 1988-07-04 |
| GB8629534D0 (en) | 1987-01-21 |
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Legal Events
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